1h6t

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Revision as of 15:57, 29 October 2007

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spinqualitylabelsall models 1h6t, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

INTERNALIN B: CRYSTAL STRUCTURE OF FUSED N-TERMINAL DOMAINS.

Overview

Listeria monocytogenes is an opportunistic, food-borne human and animal, pathogen. Host cell invasion requires the action of the internalins A, (InlA) and B (InlB), which are members of a family of listerial, cell-surface proteins. Common to these proteins are three distinctive, N-terminal domains that have been shown to direct host cell-specific, invasion for InlA and InlB. Here, we present the high-resolution crystal, structures of these domains present in InlB and InlH, and show that they, constitute a single "internalin domain". In this internalin domain, a, central LRR region is flanked contiguously by a truncated EF-hand-like cap, and an immunoglobulin (Ig)-like fold. The extended beta-sheet, resulting, from the distinctive fusion of the LRR and the Ig-like folds, constitutes, an ... [(full description)]

About this Structure

1H6T is a [Single protein] structure of sequence from [Listeria monocytogenes]. Full crystallographic information is available from [OCA].

Reference

Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain., Schubert WD, Gobel G, Diepholz M, Darji A, Kloer D, Hain T, Chakraborty T, Wehland J, Domann E, Heinz DW, J Mol Biol. 2001 Sep 28;312(4):783-94. PMID:11575932

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